Linked Life Data

8479739

Source:http://linkedlifedata.com/resource/pubmed/id/8479739

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-5-24
pubmed:abstractText
The ability of the nuclear oncoprotein Jun to activate transcription is controlled both by level of DNA binding and by the activity of its transactivation domain. Control of DNA binding is achieved by two mechanisms: phosphorylation and redox regulation. Mutation of Ser-226 inhibits phosphorylation of the DNA binding, resulting in enhanced DNA-binding and transactivation activity of Jun. In contrast, mutation of Cys-252, which is the target for repression of DNA-binding activity under oxidative conditions, results in a strong decrease of Jun-specific activation of transcription. However, transactivation by c-Jun-Cys-252 is fully restored upon mutation of Ser-226. Both mutations are also found in the oncogenic counterpart of c-Jun, v-Jun, and are the only differences between these proteins in the DNA-binding domain, suggesting that v-Jun escapes down-modulation of DNA binding by both mechanisms. However, inhibition of phosphorylation of Ser-226 is absolutely required for the ability of v-Jun to activate transcription of AP-1-dependent genes in a redox-independent manner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1141-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Mutation of a phosphorylation site in the DNA-binding domain is required for redox-independent transactivation of AP1-dependent genes by v-Jun.
pubmed:affiliation
Kernforschungszentrum Karlsruhe, Institut für Genetik, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't